3ldn
From Proteopedia
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{{STRUCTURE_3ldn| PDB=3ldn | SCENE= }} | {{STRUCTURE_3ldn| PDB=3ldn | SCENE= }} | ||
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===Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form=== | ===Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form=== | ||
| + | {{ABSTRACT_PUBMED_21526763}} | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Note=Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref> | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.<ref>PMID:2294010</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:021526763</ref><references group="xtra"/> | + | <ref group="xtra">PMID:021526763</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Dokurno, P.]] | [[Category: Dokurno, P.]] | ||
Revision as of 18:23, 24 March 2013
Contents |
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form
Template:ABSTRACT PUBMED 21526763
Disease
[GRP78_HUMAN] Note=Autoantigen in rheumatoid arthritis.[1]
Function
[GRP78_HUMAN] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.[2]
About this Structure
3ldn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Macias AT, Williamson DS, Allen N, Borgognoni J, Clay A, Daniels Z, Dokurno P, Drysdale MJ, Francis GL, Graham CJ, Howes R, Matassova N, Murray JB, Parsons R, Shaw T, Surgenor AE, Terry L, Wang Y, Wood M, Massey AJ. Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity. J Med Chem. 2011 May 20. PMID:21526763 doi:10.1021/jm101625x
- ↑ Corrigall VM, Bodman-Smith MD, Fife MS, Canas B, Myers LK, Wooley P, Soh C, Staines NA, Pappin DJ, Berlo SE, van Eden W, van Der Zee R, Lanchbury JS, Panayi GS. The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis. J Immunol. 2001 Feb 1;166(3):1492-8. PMID:11160188
- ↑ Dana RC, Welch WJ, Deftos LJ. Heat shock proteins bind calcitonin. Endocrinology. 1990 Jan;126(1):672-4. PMID:2294010
Categories: Homo sapiens | Dokurno, P. | Macias, A T. | Massey, A J. | Shaw, T. | Surgenor, A E. | Williamson, D S. | Adenosine | Atp-binding | Chaperone | Endoplasmic reticulum | Grp78 | Heat shock | Hsc70 | Hsp70 | Nucleoside | Nucleotide-binding | Phosphoprotein | Protein folding | Selectivity | Small molecule inhibitor | Stress response
